Novel secreted isoform of adhesion molecule ICAM-4: potential regulator of membrane-associated ICAM-4 interactions

Lee, Gloria; Spring, Frances A.; Parsons, Stephen; Mankelow, Tosti J.; Peters, Luanne L.; Koury, Mark J.; Mohandas, Narla; Anstee, David J.; Chasis, Joel Anne

doi:10.1182/blood-2002-08-2529

Cited by 41 publications

(31 citation statements)

References 35 publications

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“…Thus, it is not surprising that various functional impairments described in either macrophages or Ebs are mainly manifested under stress. Molecules providing adhesive contact between macrophages and Ebs (alpha4 integrin/VCAM-1, 8,19,20 ICAM4/alphav/alpha4 integrins, 10,11,21,22 CD163, 23 palladin, 12 as well as extracellular matrix proteins, fibronectin, 24,25 and laminin), [26][27][28] exert regulatory roles mostly under stress by influencing growth, differentiation, and adhesion/migration of erythroid cells. In addition to direct contact, soluble factors secreted by either Ebs or macrophages influence stress erythropoiesis.…”

Section: Introductionmentioning

confidence: 99%

The macrophage contribution to stress erythropoiesis: when less is enough

Ulyanova

Phelps

Papayannopoulou

2016

Blood

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• Significant expansion only of native splenic macrophages that are F4/80 1 /Cd11b lo occurs in both post-Epo and post-hemolysis-induced stress.• VCAM-1 2/2 mice, like Spi-C 2/2 , mice have significantly decreased macrophages but did not have a compromised E-stress response.Although the importance of native bone marrow and spleen macrophages in enhancing baseline and stress erythropoiesis has been emphasized over several decades, their kinetic and phenotypic changes during a variety of stress responses have been unclear. Furthermore, whether monocyte-derived recruited macrophages can functionally substitute for inadequate or functionally impaired native macrophages has been controversial and seem to be not only tissue-but also stress-type dependent. To provide further insight into these issues, we made detailed observations at baseline and post-erythroid stress (E-stress) in 2 mouse models with genetically depressed macrophage numbers and compared them to their controls. We documented that, irrespective of the stressinduced (hemolytic or post-erythropoietin [Epo]) treatment, only native CD11b lo splenic macrophages expand dramatically post-stress in normal mice without significant changes in the monocyte-derived CD11b hi subset. The latter remained a minority and did not change post-stress in 2 genetic models lacking either Spi-C or VCAM-1 with impaired native macrophage proliferative expansion. Although CD11b lo macrophages in these mice were one-fifth of normal at their peak response, surprisingly, their erythroid response was not compromised and was similar to controls. Thus, despite the prior emphasis on numerical macrophage reliance to provide functional rescue from E-stress, our data highlight the importance of previously described non-macrophage-dependent pathways activated under certain stress conditions to compensate for low macrophage numbers. (Blood. 2016;128(13):1756-1765

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Section: Introductionmentioning

confidence: 99%

The macrophage contribution to stress erythropoiesis: when less is enough

Ulyanova

Phelps

Papayannopoulou

2016

Blood

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“…Erythroblasts are organized into erythroblastic islands that consist of macrophages surrounded by developing erythroid precursors. 144,145 Macrophages provide many of the cellular mediators that control erythropoietic activity: GM-CSF, IL-3, and stem cell factor (SCF) generate colony-forming unit erythroid macrophage-granulocyte megakaryocyte (CFU-GEMM) and burst-forming unit erythroid (BFU-E), whereas TGF-␤, TNF-␣, and MIP1-␣ inhibit cell cycle activity 146 and BFU-E development. Other factors that negatively regulate numbers include proapoptotic activity initiated by interaction of the Fas receptor (CD95) with Fas ligand (CD95L).…”

Section: Erythropoietic Suppression and Dyserythropoiesismentioning

confidence: 99%

Malarial anemia: of mice and men

Lamikanra

Brown²,

Potocnik³

et al. 2007

Blood

229

215

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Severe malaria is manifest by a variety of clinical syndromes dependent on properties of both the host and the parasite. In young infants, severe malarial anemia (SMA) is the most common syndrome of severe disease and contributes substantially to the considerable mortality and morbidity from malaria. There is now growing evidence, from both human and mouse studies of malaria, to show that anemia is due not only to increased hemolysis of infected and clearance of uninfected red blood cells (RBCs) but also to an inability of the infected host to produce an adequate erythroid response. In this review, we will summarize the recent clinical and experimental studies of malaria to highlight similarities and differences in human and mouse pathology that result in anemia and so inform the use of mouse models in the study of severe malarial anemia in humans. Malaria in humansThe vast majority of morbidity and mortality from malaria is caused by infection with Plasmodium falciparum, although P vivax, P ovale, and P malariae also are responsible for human infections. The total burden of disease has recently been estimated to 515 million episodes annually and malaria is responsible for 18% of all childhood deaths in sub-Saharan Africa, equivalent to 800 000 deaths each year. 1,2 The study of malarial anemia has somewhat belatedly excited academic and professional interest. Severe malarial anemia (SMA) certainly merits concern as a major public health problem because of the very large numbers of children affected, and it is likely that these numbers may increase as drug resistance spreads. Concerns have also been raised by data from recent vaccine studies, which suggest that monkeys immunized with erythrocytic-stage antigens, and that have acquired protection from acute infection, may succumb to severe anemia during a subacute or chronic phase of infection. 3,4 Moreover, there is increasing awareness of the difficulty of satisfactory treatment by blood transfusion outside specialist centers in many endemic areas as a result of the limited availability of a rapid and safe supply of blood. 1,5 SMA is seen most frequently in areas of very high malaria transmission and most commonly in young children and pregnant women. 6 The prevalence of anemia, defined as a hematocrit (Hct) level higher than 0.33, in malaria-endemic areas of Africa, varies between 31% and 91% in children, and between 60% and 80% in pregnant women. 7,8 Given the high degree of morbidity that is associated with SMA in children, this term will be used to refer to severe anemia in this group, unless stated otherwise.It is very difficult to determine the number of cases of severe anemia attributable to malaria as the WHO definition of SMA (a hemoglobin [Hb] concentration of Ͻ 50 g/L [5 g/dL], or a Hct Ͻ 0.15, in the presence of a parasitemia Ͼ 10 000 parasites per microliter [L], and a normocytic blood film) may exclude the considerable proportion of children admitted with severe anemia that has a blood smear negative for malaria parasites but that responds to an...

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“…This is achieved either by protease-mediated cleavage of the extracellular domains near the plasma membrane (Pigott et al, 1992;Hahne et al, 1994) or by alternative splicing of mRNA transcribed from a single gene (Budt et al, 2002;Lee et al, 2003). Soluble forms often inhibit the adhesive functions of the corresponding membrane-bound forms by binding to their extracellular domains (Kaplan et al, 1993;Meyer et al, 1995;Budt et al, 2002).…”

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confidence: 99%

Cloning of a soluble isoform of the SgIGSF adhesion molecule that binds the extracellular domain of the membrane-bound isoform

et al. 2004

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SgIGSF (spermatogenic immunoglobulin superfamily) is a recently identified intercellular adhesion molecule of the immunoglobulin superfamily. In a mast-cell cDNA library, we found a clone that resulted from the retention of intron 7 within the mature SgIGSF message. This clone was predicted to encode a soluble isoform of SgIGSF (sSgIGSF) with 336 amino-acid residues because its open reading frame ended just before the transmembrane domain. We constructed a plasmid expressing sSgIGSF fused to the human IgG Fc fragment at its C-terminus (sSgIGSF-Fc), and transfected it into COS-7 cells. The fusion protein was readily detectable in the culture supernatant. Solid-phase binding assay showed that sSgIGSF interacted directly the extracellular domain of membrane-bound SgIGSF (mSgIGSF). We next examined whether this interaction inhibited homophilic binding of mSgIGSF by aggregation assays using L cells that did not express mSgIGSF. A stable L-cell clone that overexpressed mSgIGSF aggregated with each other but not with mock-transfected L cells, indicating that a homophilic interaction of mSgIGSF mediated the aggregation. Addition of sSgIGSF-Fc inhibited the aggregation of L cells overexpressing mSgIGSF in a dose-dependent manner. Moreover, FACScan analyses revealed the specific binding of sSgIGSF-Fc to mSgIGSF expressed in L cells. Binding of sSgIGSF-Fc to mSgIGSF appeared to inhibit homophilic interactions of mSgIGSF.

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Novel secreted isoform of adhesion molecule ICAM-4: potential regulator of membrane-associated ICAM-4 interactions

Cited by 41 publications

References 35 publications

The macrophage contribution to stress erythropoiesis: when less is enough

The macrophage contribution to stress erythropoiesis: when less is enough

Malarial anemia: of mice and men

Cloning of a soluble isoform of the SgIGSF adhesion molecule that binds the extracellular domain of the membrane-bound isoform

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